TFR1_CHICK
ID TFR1_CHICK Reviewed; 776 AA.
AC Q90997;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-FEB-2002, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Transferrin receptor protein 1;
DE Short=TR;
DE Short=TfR;
DE Short=TfR1;
DE Short=Trfr;
GN Name=TFRC;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Erythroblast, and Lymphoma;
RX PubMed=1874449; DOI=10.1016/0378-1119(91)90085-p;
RA Gerhardt E.M., Chan L.-N.L., Jing S., Qi M., Trowbridge I.S.;
RT "The cDNA sequence and primary structure of the chicken transferrin
RT receptor.";
RL Gene 102:249-254(1991).
CC -!- FUNCTION: Cellular uptake of iron occurs via receptor-mediated
CC endocytosis of ligand-occupied transferrin receptor into specialized
CC endosomes (By similarity). Endosomal acidification leads to iron
CC release. The apotransferrin-receptor complex is then recycled to the
CC cell surface with a return to neutral pH and the concomitant loss of
CC affinity of apotransferrin for its receptor. Transferrin receptor is
CC necessary for development of erythrocytes and the nervous system (By
CC similarity). Acts as a lipid sensor that regulates mitochondrial fusion
CC by regulating activation of the JNK pathway (By similarity). When
CC dietary levels of stearate (C18:0) are low, promotes activation of the
CC JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent
CC degradation of the mitofusin MFN2 and inhibition of mitochondrial
CC fusion (By similarity). When dietary levels of stearate (C18:0) are
CC high, TFRC stearoylation inhibits activation of the JNK pathway and
CC thus degradation of the mitofusin MFN2 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Binds one transferrin molecule
CC per subunit (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P02786};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:P02786}.
CC Melanosome {ECO:0000250|UniProtKB:P02786}.
CC -!- PTM: Stearoylated (By similarity). Stearoylation does not affect iron
CC uptake (By similarity). {ECO:0000250|UniProtKB:P02786}.
CC -!- PTM: N- and O-glycosylated, phosphorylated and palmitoylated.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA39035.1; Type=Frameshift; Note=The correct sequence is shown in fig.1 of PubMed:1874449.; Evidence={ECO:0000305};
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DR EMBL; X55348; CAA39035.1; ALT_FRAME; mRNA.
DR PIR; JH0570; JH0570.
DR RefSeq; NP_990587.2; NM_205256.2.
DR AlphaFoldDB; Q90997; -.
DR SMR; Q90997; -.
DR STRING; 9031.ENSGALP00000012087; -.
DR MEROPS; M28.972; -.
DR PaxDb; Q90997; -.
DR GeneID; 396191; -.
DR KEGG; gga:396191; -.
DR CTD; 7037; -.
DR VEuPathDB; HostDB:geneid_396191; -.
DR eggNOG; KOG2195; Eukaryota.
DR InParanoid; Q90997; -.
DR OrthoDB; 804230at2759; -.
DR PhylomeDB; Q90997; -.
DR PRO; PR:Q90997; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0004998; F:transferrin receptor activity; ISS:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:UniProtKB.
DR GO; GO:0045830; P:positive regulation of isotype switching; ISS:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:0033572; P:transferrin transport; ISS:UniProtKB.
DR CDD; cd02128; PA_TfR; 1.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR029513; TfR.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR InterPro; IPR037324; TfR1/2_PA.
DR PANTHER; PTHR10404; PTHR10404; 1.
DR PANTHER; PTHR10404:SF26; PTHR10404:SF26; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endocytosis; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..776
FT /note="Transferrin receptor protein 1"
FT /id="PRO_0000174135"
FT TOPO_DOM 1..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..776
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 230..322
FT /note="PA"
FT REGION 586..776
FT /note="Ligand-binding"
FT /evidence="ECO:0000250"
FT MOTIF 19..22
FT /note="Endocytosis signal"
FT MOTIF 662..664
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT LIPID 70
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P02786"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P02786"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 738
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 101
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VARIANT 581
FT /note="R -> H (in bursal lymphoma)"
FT VARIANT 736
FT /note="K -> Q (in bursal lymphoma)"
SQ SEQUENCE 776 AA; 85659 MW; DB293BAC41ED0623 CRC64;
MDHARAALSN LFSVEPMSYT RFSIARQTDG DNSHVEMKLS ADDEEGGDIE RPEHMHVSMA
QPQRNGKRLC FLVIAAVLLL LIGFLIGYLS YRGRIELAAR CQDGSGGCEI TPTASYLVDG
EGTVEEEIQG PPVIFWPELK AMLSKKLSAK NLVDNLRWRV GVDSFEAGEA EDTNMATYIH
EEFRNFLDKV WNDEHYIKLQ VRGSTKNQVS ISINGKEEIL ETPDAIVAYS ESGSVSGKPV
YVNYGLKKDF EIIQKVVASL NGTIVIVRAG KITLAEKVAN AKEAGAAGVL MYVDSLMYGI
TDTLIPFGHA HLGTGDPYTP GFPSFNHTQF PPVESSGLPH IAVQTISSSA AARLFSKMDG
DTCSEGWKGA IHSCKVTTKQ ESQIMVKLDV NNSMKDRKIL NIFGAIQGFE EPDRYVVIGA
QRDSWGPGVA KAGTGTAILL ELARVISDIV KNEGYKPRRS IIFASWSAGD YGAVGATEWL
EGYSAMLHAK AFTYISLDAP VLGASHVKIS ASPLLYMLLG SIMKGVKNPA AVSESLYNRL
GPDWVKAVVP LGLDNAAFPF LAYSGIPVLS FGFYNKDEEY RFLDTKGDTL ENLRKIDNLD
ALLAAAAEVA GQAALRLTHD HELFLDIGRY SEELLAYQEE FLPYIKEVRE LGLTLDWLFF
ARGDFQRAVT ALRRDIANSD GENRVIRRAL NDRMMKVEYD FLSPYLSPKD VPFRHIFFGK
GPHTLRSLVE HLQLLKTNRS SVDLNLLREQ LALATWTIKG AANALGGDIW ETDNEF
